(1S,2S,6R,8S)-4-[(1S)-1-chloroethyl]-2,9,9-trimethyl-3,5-dioxa-4-boratricyclo[6.1.1.02,6]decane | 85167-12-0

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: (1S,2S,6R,8S)-4-[(1S)-1-chloroethyl]-2,9,9-trimethyl-3,5-dioxa-4-boratricyclo[6.1.1.02,6]decane
• CAS: 85167-12-0
• 化学式: C₁₂H₂₀BClO₂
• 分子量: 242.554
• InChiKey: LNJGJPHOEZVFMM-LNGZZDABSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.88
• 重原子数：
  16
• 可旋转键数：
  1
• 环数：
  4.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  18.5
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  (1S,2S,6R,8S)-4-[(1S)-1-chloroethyl]-2,9,9-trimethyl-3,5-dioxa-4-boratricyclo[6.1.1.02,6]decane 在 N-甲基吗啉 、 盐酸 、 1-羟基苯并三唑 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 正己烷 、 二氯甲烷 为溶剂， 生成
  参考文献：
  名称：

  Boro-norleucine as a P1 residue for the design of selective and potent DPP7 inhibitors

  摘要：

  Dipeptide-based inhibitors with C-substituted (alkyl or aminoalkyl) alpha-amino acids in the P2 position and born-norleucine (boro-Nle) in the P1 position were synthesized. Relative to born-proline, boro-Nle as a P1 residue was shown able to significantly dial out DPP4, FAP, DPP8, and DPP9 activity. Dab-boro-Nle (4g) proved to be the most selective and potent DPP7 inhibitor with a DPP7 IC50 value of 480 pM. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2005.06.076
• 作为产物：
  描述：

  (1S,2S,3R,5S)-(+)-2,3-蒎烷二醇 在 zinc(II) chloride 作用下， 以 四氢呋喃 、 乙醚 为溶剂， 生成 (1S,2S,6R,8S)-4-[(1S)-1-chloroethyl]-2,9,9-trimethyl-3,5-dioxa-4-boratricyclo[6.1.1.02,6]decane
  参考文献：
  名称：

  Boro-norleucine as a P1 residue for the design of selective and potent DPP7 inhibitors

  摘要：

  Dipeptide-based inhibitors with C-substituted (alkyl or aminoalkyl) alpha-amino acids in the P2 position and born-norleucine (boro-Nle) in the P1 position were synthesized. Relative to born-proline, boro-Nle as a P1 residue was shown able to significantly dial out DPP4, FAP, DPP8, and DPP9 activity. Dab-boro-Nle (4g) proved to be the most selective and potent DPP7 inhibitor with a DPP7 IC50 value of 480 pM. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2005.06.076

文献信息

• [EN] BETA-LACTAMASE INHIBITORS<br/>[FR] INHIBITEURS DE BÊTA-LACTAMASE
  申请人：UNIV CALIFORNIA

  公开号：WO2013056163A1

  公开（公告）日：2013-04-18

  Disclosed herein inter alia are Boron containing compounds and methods for treating infections related to antibiotic resistant microorganisms.

  本公开涉及含硼化合物和治疗与抗生素耐药微生物相关感染的方法。
• 99% Chirally selective synthesis via pinanediol boronic esters: insect pheromones, diols, and an amino alcohol
  作者：Donald S. Matteson、Kizhakethil Mathew. Sadhu、Mark L. Peterson

  DOI：10.1021/ja00264a039

  日期：1986.2

  Synthese en particulier du methyl-4 heptanol-3, brevicomine, eldanolide, decanediol-5,6, methyl-6 undecanediol-5,7 et amino-6 decanol-5

  合成这些特别是甲基-4 庚醇-3、短苯胺、eldanolide、癸二醇-5,6、甲基-6 十一烷二醇-5,7 和氨基-6 癸醇-5
• Probing the Specificity of the Serine Proteases Subtilisin Carlsberg and α-Chymotrypsin with Enantiomeric 1-Acetamido Boronic Acids. An Unexpected Reversal of the Normal “<scp>l</scp>”-Stereoselectivity Preference
  作者：Valeri Martichonok、J. Bryan Jones

  DOI：10.1021/ja952816j

  日期：1996.1.1

  Enantiomeric 1-acetamido boronic acids, which are N-acetyl transition state analog inhibitor analogs of L- and D-forms of the amino acids alanine, phenylalanine, p-fluorophenylalanine, p-chlorophenylalanine, and 1-naphthylalanine, have been evaluated as inhibitors of the serine proteases subtilisin Carlsberg (SC) and alpha-chymotrypsin (CT). All of the boronic acids are powerful competitive inhibitors of both enzymes, with, as expected, the L-enantiomers being generally more potent than the D-enantiomers. However, a dramatic reversal of the normal stereoselectivity preference was observed in the inhibition of CT by [1-acetamido-2-(1-naphthyl)ethyl]boronic acid, with the D-enantiomer becoming a 25-fold more potent inhibitor than the L-enantiomer. Furthermore, the K-I of 127 nM for CT inhibition by this D-enantiomer is the lowest of any of the boronic acids evaluated. Molecular modeling analyses of the possible binding modes of the inhibitors suggest that the stereoselectivity reversal is due to S-1-pocket orientations of naphthyl groups that are different from those of the aromatic side chains of the phenylalanine analogs.
• Characterization of d-boroAla as a Novel Broad-Spectrum Antibacterial Agent Targeting d-Ala-d-Ala Ligase
  作者：Sandeep Putty、Aman Rai、Darshan Jamindar、Paul Pagano、Cheryl L. Quinn、Takehiko Mima、Herbert P. Schweizer、William G. Gutheil

  DOI：10.1111/j.1747-0285.2011.01210.x

  日期：2011.11

  d‐boroAla was previously characterized as an inhibitor of bacterial alanine racemase and d‐Ala‐d‐Ala ligase enzymes (Biochemistry, 28, 1989, 3541). In this study, d‐boroAla was identified and characterized as an antibacterial agent. d‐boroAla has activity against both Gram‐positive and Gram‐negative organisms, with minimal inhibitory concentrations down to 8 μg / mL. A structure–function study on the alkyl side chain (NH2‐CHR‐B(OR’)2) revealed that d‐boroAla is the most effective agent in a series including boroGly, d‐boroHomoAla, and d‐boroVal. l‐boroAla was much less active, and N‐acetylation completely abolished activity. An LC‐MS / MS assay was used to demonstrate that d‐boroAla exerts its antibacterial activity by inhibition of d‐Ala‐d‐Ala ligase. d‐boroAla is bactericidal at 1× minimal inhibitory concentration against Staphylococcus aureus and Bacillus subtilis, which each encode one copy of d‐Ala‐d‐Ala ligase, and at 4× minimal inhibitory concentration against Escherichia coli and Salmonella enterica serovar Typhimurium, which each encode two copies of d‐Ala‐d‐Ala ligase. d‐boroAla demonstrated a frequency of resistance of 8 × 10−8 at 4× minimal inhibitory concentration in S. aureus. These results demonstrate that d‐boroAla has promising antibacterial activity and could serve as the lead agent in a new class of d‐Ala‐d‐Ala ligase targeted antibacterial agents. This study also demonstrates d‐boroAla as a possible probe for d‐Ala‐d‐Ala ligase function.
• Matteson, Donald S.; Jesthi, Pradipta K.; Sadhu, Kizhakethil M., Organometallics, 1984, vol. 3, # 8, p. 1284 - 1288
  作者：Matteson, Donald S.、Jesthi, Pradipta K.、Sadhu, Kizhakethil M.

  DOI：——

  日期：——